Structural transition temperature of hemoglobins correlates with species' body temperature
Human red blood cells (RBCs) exhibit sudden changes in their biophysical properties at body temperature (T (B)). RBCs were seen to undergo a spontaneous transition from blockage to passage at T (C) = 36.4 +/- 0.3 degrees C, when the temperature dependency of RBC-passages through 1.3 mum narrow micro...
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| Veröffentlicht in: | European biophysics journal 2007-12, Vol.37 (1), p.1-10 |
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| creator | Zerlin, Kay Frank Thorsten Kasischke, Nicole Digel, Ilya Maggakis-Kelemen, Christina Temiz Artmann, Aysegül Porst, Dariusz Kayser, Peter Linder, Peter Artmann, Gerhard Michael |
| description | Human red blood cells (RBCs) exhibit sudden changes in their biophysical properties at body temperature (T (B)). RBCs were seen to undergo a spontaneous transition from blockage to passage at T (C) = 36.4 +/- 0.3 degrees C, when the temperature dependency of RBC-passages through 1.3 mum narrow micropipettes was observed. Moreover, concentrated hemoglobin solutions (45 g/dl) showed a viscosity breakdown between 36 and 37 degrees C. With human hemoglobin, a structural transition was observed at T (B) as circular dichroism (CD) experiments revealed. This leads to the assumption that a species' body temperature occupies a unique position on the temperature scale and may even be imprinted in the structure of certain proteins. In this study, it was investigated whether hemoglobins of species with a T (B) different from those of human show temperature transitions and whether those were also linked to the species' T (B). The main conclusion was drawn from dynamic light scattering (DLS) and CD experiments. It was observed that such structural temperature transitions did occur in hemoglobins from all studied species and were correlated linearly (slope 0.81, r = 0.95) with the species' body temperature. We presumed that alpha-helices of hemoglobin were able to unfold more readily around T (B). alpha-helical unfolding would initiate molecular aggregation causing RBC passage and viscosity breakdown as mentioned above. Thus, structural molecular changes of hemoglobin could determine biophysical effects visible on a macroscopic scale. It is hypothesized that the species' body temperature was imprinted into the structure of hemoglobins. |
| doi_str_mv | 10.1007/s00249-007-0144-4 |
| format | Article |
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RBCs were seen to undergo a spontaneous transition from blockage to passage at T (C) = 36.4 +/- 0.3 degrees C, when the temperature dependency of RBC-passages through 1.3 mum narrow micropipettes was observed. Moreover, concentrated hemoglobin solutions (45 g/dl) showed a viscosity breakdown between 36 and 37 degrees C. With human hemoglobin, a structural transition was observed at T (B) as circular dichroism (CD) experiments revealed. This leads to the assumption that a species' body temperature occupies a unique position on the temperature scale and may even be imprinted in the structure of certain proteins. In this study, it was investigated whether hemoglobins of species with a T (B) different from those of human show temperature transitions and whether those were also linked to the species' T (B). The main conclusion was drawn from dynamic light scattering (DLS) and CD experiments. It was observed that such structural temperature transitions did occur in hemoglobins from all studied species and were correlated linearly (slope 0.81, r = 0.95) with the species' body temperature. We presumed that alpha-helices of hemoglobin were able to unfold more readily around T (B). alpha-helical unfolding would initiate molecular aggregation causing RBC passage and viscosity breakdown as mentioned above. Thus, structural molecular changes of hemoglobin could determine biophysical effects visible on a macroscopic scale. It is hypothesized that the species' body temperature was imprinted into the structure of hemoglobins.</description><identifier>ISSN: 0175-7571</identifier><identifier>EISSN: 1432-1017</identifier><identifier>DOI: 10.1007/s00249-007-0144-4</identifier><identifier>PMID: 17390129</identifier><language>eng</language><publisher>Germany: Springer Nature B.V</publisher><subject>Animals ; Body temperature ; Body Temperature - physiology ; Computer Simulation ; Hemoglobin ; Hemoglobins - chemistry ; Hemoglobins - physiology ; Hemoglobins - ultrastructure ; Humans ; Light scattering ; Models, Biological ; Models, Chemical ; Phase Transition ; Protein Conformation ; Species Specificity ; Temperature ; Transition temperatures</subject><ispartof>European biophysics journal, 2007-12, Vol.37 (1), p.1-10</ispartof><rights>EBSA 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c326t-f774fb4aabdb855d1eca71aaf21fd074893a728fbc4ab34b4ec471fd28d06b903</citedby><cites>FETCH-LOGICAL-c326t-f774fb4aabdb855d1eca71aaf21fd074893a728fbc4ab34b4ec471fd28d06b903</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17390129$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zerlin, Kay Frank Thorsten</creatorcontrib><creatorcontrib>Kasischke, Nicole</creatorcontrib><creatorcontrib>Digel, Ilya</creatorcontrib><creatorcontrib>Maggakis-Kelemen, Christina</creatorcontrib><creatorcontrib>Temiz Artmann, Aysegül</creatorcontrib><creatorcontrib>Porst, Dariusz</creatorcontrib><creatorcontrib>Kayser, Peter</creatorcontrib><creatorcontrib>Linder, Peter</creatorcontrib><creatorcontrib>Artmann, Gerhard Michael</creatorcontrib><title>Structural transition temperature of hemoglobins correlates with species' body temperature</title><title>European biophysics journal</title><addtitle>Eur Biophys J</addtitle><description>Human red blood cells (RBCs) exhibit sudden changes in their biophysical properties at body temperature (T (B)). RBCs were seen to undergo a spontaneous transition from blockage to passage at T (C) = 36.4 +/- 0.3 degrees C, when the temperature dependency of RBC-passages through 1.3 mum narrow micropipettes was observed. Moreover, concentrated hemoglobin solutions (45 g/dl) showed a viscosity breakdown between 36 and 37 degrees C. With human hemoglobin, a structural transition was observed at T (B) as circular dichroism (CD) experiments revealed. This leads to the assumption that a species' body temperature occupies a unique position on the temperature scale and may even be imprinted in the structure of certain proteins. In this study, it was investigated whether hemoglobins of species with a T (B) different from those of human show temperature transitions and whether those were also linked to the species' T (B). The main conclusion was drawn from dynamic light scattering (DLS) and CD experiments. It was observed that such structural temperature transitions did occur in hemoglobins from all studied species and were correlated linearly (slope 0.81, r = 0.95) with the species' body temperature. We presumed that alpha-helices of hemoglobin were able to unfold more readily around T (B). alpha-helical unfolding would initiate molecular aggregation causing RBC passage and viscosity breakdown as mentioned above. Thus, structural molecular changes of hemoglobin could determine biophysical effects visible on a macroscopic scale. It is hypothesized that the species' body temperature was imprinted into the structure of hemoglobins.</description><subject>Animals</subject><subject>Body temperature</subject><subject>Body Temperature - physiology</subject><subject>Computer Simulation</subject><subject>Hemoglobin</subject><subject>Hemoglobins - chemistry</subject><subject>Hemoglobins - physiology</subject><subject>Hemoglobins - ultrastructure</subject><subject>Humans</subject><subject>Light scattering</subject><subject>Models, Biological</subject><subject>Models, Chemical</subject><subject>Phase Transition</subject><subject>Protein Conformation</subject><subject>Species Specificity</subject><subject>Temperature</subject><subject>Transition temperatures</subject><issn>0175-7571</issn><issn>1432-1017</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkE9LxDAQxYMo7rr6AbxI8aCnaiZJm_Yoi_9gwYN68RKSNHG7tE1NUmS_vS27oHiZGWbeeww_hM4B3wDG_DZgTFiZjmOKgbGUHaA5MEpSwMAP0XysWcozDjN0EsIGY5YBFMdoBpyWGEg5Rx-v0Q86Dl42SfSyC3WsXZdE0_bGy3FvEmeTtWndZ-NU3YVEO-9NI6MJyXcd10noja5NuE6Uq7Z_jafoyMommLN9X6D3h_u35VO6enl8Xt6tUk1JHlPLObOKSakqVWRZBUZLDlJaArbCnBUllZwUVmkmFWWKGc34eCJFhXNVYrpAV7vc3ruvwYQo2jpo0zSyM24IIi8yQoGzUXj5T7hxg-_G30ROOM5GpnQUwU6kvQvBGyt6X7fSbwVgMVEXO-piGifqYgq-2AcPqjXVr2OPmf4Aiuh_Vg</recordid><startdate>20071201</startdate><enddate>20071201</enddate><creator>Zerlin, Kay Frank Thorsten</creator><creator>Kasischke, Nicole</creator><creator>Digel, Ilya</creator><creator>Maggakis-Kelemen, Christina</creator><creator>Temiz Artmann, Aysegül</creator><creator>Porst, Dariusz</creator><creator>Kayser, Peter</creator><creator>Linder, Peter</creator><creator>Artmann, Gerhard Michael</creator><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20071201</creationdate><title>Structural transition temperature of hemoglobins correlates with species' body temperature</title><author>Zerlin, Kay Frank Thorsten ; Kasischke, Nicole ; Digel, Ilya ; Maggakis-Kelemen, Christina ; Temiz Artmann, Aysegül ; Porst, Dariusz ; Kayser, Peter ; Linder, Peter ; Artmann, Gerhard Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c326t-f774fb4aabdb855d1eca71aaf21fd074893a728fbc4ab34b4ec471fd28d06b903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Body temperature</topic><topic>Body Temperature - 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Academic</collection><jtitle>European biophysics journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zerlin, Kay Frank Thorsten</au><au>Kasischke, Nicole</au><au>Digel, Ilya</au><au>Maggakis-Kelemen, Christina</au><au>Temiz Artmann, Aysegül</au><au>Porst, Dariusz</au><au>Kayser, Peter</au><au>Linder, Peter</au><au>Artmann, Gerhard Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural transition temperature of hemoglobins correlates with species' body temperature</atitle><jtitle>European biophysics journal</jtitle><addtitle>Eur Biophys J</addtitle><date>2007-12-01</date><risdate>2007</risdate><volume>37</volume><issue>1</issue><spage>1</spage><epage>10</epage><pages>1-10</pages><issn>0175-7571</issn><eissn>1432-1017</eissn><abstract>Human red blood cells (RBCs) exhibit sudden changes in their biophysical properties at body temperature (T (B)). RBCs were seen to undergo a spontaneous transition from blockage to passage at T (C) = 36.4 +/- 0.3 degrees C, when the temperature dependency of RBC-passages through 1.3 mum narrow micropipettes was observed. Moreover, concentrated hemoglobin solutions (45 g/dl) showed a viscosity breakdown between 36 and 37 degrees C. With human hemoglobin, a structural transition was observed at T (B) as circular dichroism (CD) experiments revealed. This leads to the assumption that a species' body temperature occupies a unique position on the temperature scale and may even be imprinted in the structure of certain proteins. In this study, it was investigated whether hemoglobins of species with a T (B) different from those of human show temperature transitions and whether those were also linked to the species' T (B). The main conclusion was drawn from dynamic light scattering (DLS) and CD experiments. It was observed that such structural temperature transitions did occur in hemoglobins from all studied species and were correlated linearly (slope 0.81, r = 0.95) with the species' body temperature. We presumed that alpha-helices of hemoglobin were able to unfold more readily around T (B). alpha-helical unfolding would initiate molecular aggregation causing RBC passage and viscosity breakdown as mentioned above. Thus, structural molecular changes of hemoglobin could determine biophysical effects visible on a macroscopic scale. It is hypothesized that the species' body temperature was imprinted into the structure of hemoglobins.</abstract><cop>Germany</cop><pub>Springer Nature B.V</pub><pmid>17390129</pmid><doi>10.1007/s00249-007-0144-4</doi><tpages>10</tpages></addata></record> |
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| subjects | Animals Body temperature Body Temperature - physiology Computer Simulation Hemoglobin Hemoglobins - chemistry Hemoglobins - physiology Hemoglobins - ultrastructure Humans Light scattering Models, Biological Models, Chemical Phase Transition Protein Conformation Species Specificity Temperature Transition temperatures |
| title | Structural transition temperature of hemoglobins correlates with species' body temperature |
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